RIR2A_MYCTU
ID RIR2A_MYCTU Reviewed; 322 AA.
AC P9WH73; L0TAZ9; Q10840; Q50548;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta nrdF1;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase R2-1 small subunit;
DE AltName: Full=Ribonucleotide reductase small subunit 1;
GN Name=nrdF1; OrderedLocusNames=Rv1981c; ORFNames=MTCY39.38;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND LACK OF FUNCTION IN
RP E.COLI.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=9335290; DOI=10.1128/jb.179.20.6408-6415.1997;
RA Yang F., Curran S.C., Li L.S., Avarbock D., Graf J.D., Chua M.M., Lu G.,
RA Salem J., Rubin H.;
RT "Characterization of two genes encoding the Mycobacterium tuberculosis
RT ribonucleotide reductase small subunit.";
RL J. Bacteriol. 179:6408-6415(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14573627; DOI=10.1128/iai.71.11.6124-6131.2003;
RA Dawes S.S., Warner D.F., Tsenova L., Timm J., McKinney J.D., Kaplan G.,
RA Rubin H., Mizrahi V.;
RT "Ribonucleotide reduction in Mycobacterium tuberculosis: function and
RT expression of genes encoding class Ib and class II ribonucleotide
RT reductases.";
RL Infect. Immun. 71:6124-6131(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). Two genes for this
CC protein are present in M.tuberculosis; this is thought to not be the
CC active form. When coexpressed in E.coli with nrdE the 2 proteins do not
CC complement a temperature-sensitive E.coli mutant, whereas the other
CC gene (nrdF2) does complement. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- INDUCTION: Expressed in growing cells (at protein level). Transcription
CC not induced under oxygen-limiting conditions.
CC {ECO:0000269|PubMed:14573627}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; U41099; AAB81405.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44750.1; -; Genomic_DNA.
DR PIR; C70756; C70756.
DR RefSeq; WP_003899116.1; NZ_NVQJ01000048.1.
DR RefSeq; YP_177853.1; NC_000962.3.
DR AlphaFoldDB; P9WH73; -.
DR SMR; P9WH73; -.
DR STRING; 83332.Rv1981c; -.
DR PaxDb; P9WH73; -.
DR GeneID; 885923; -.
DR KEGG; mtu:Rv1981c; -.
DR TubercuList; Rv1981c; -.
DR eggNOG; COG0208; Bacteria.
DR OMA; LMESAMI; -.
DR PhylomeDB; P9WH73; -.
DR BRENDA; 1.17.4.1; 3445.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR026494; RNR_NrdF-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR04171; RNR_1b_NrdF; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 1: Evidence at protein level;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..322
FT /note="Ribonucleoside-diphosphate reductase subunit beta
FT nrdF1"
FT /id="PRO_0000190486"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 70
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 151..155
FT /note="LKRKA -> QAQR (in Ref. 1; AAB81405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 36590 MW; 320B939E259E4432 CRC64;
MTGKLVERVH AINWNRLLDA KDLQVWERLT GNFWLPEKIP LSNDLASWQT LSSTEQQTTI
RVFTGLTLLD TAQATVGAVA MIDDAVTPHE EAVLTNMAFM ESVHAKSYSS IFSTLCSTKQ
IDDAFDWSEQ NPYLQRKAQI IVDYYRGDDA LKRKASSVML ESFLFYSGFY LPMYWSSRGK
LTNTADLIRL IIRDEAVHGY YIGYKCQRGL ADLTDAERAD HREYTCELLH TLYANEIDYA
HDLYDELGWT DDVLPYMRYN ANKALANLGY QPAFDRDTCQ VNPAVRAALD PGAGENHDFF
SGSGSSYVMG THQPTTDTDW DF
